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Protein

Citrate lyase subunit beta-like protein, mitochondrial

Gene

Clybl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial malate and beta-methylmalate synthase, which may be involved in vitamin B12 metabolism. Acts both as a malate synthase, converting glyoxylate and acetyl-CoA to malate. Also acts as a beta-methylmalate synthase by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate.By similarity

Catalytic activityi

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA.By similarity
Propionyl-CoA + H2O + glyoxylate = beta-methylmalate + CoA.By similarity

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051SubstrateBy similarity
Metal bindingi169 – 1691MagnesiumBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Metal bindingi204 – 2041MagnesiumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.1.3.6. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate lyase subunit beta-like protein, mitochondrial
Short name:
Citrate lyase beta-like
Alternative name(s):
Beta-methylmalate synthase (EC:2.3.3.-By similarity)
Malate synthase (EC:2.3.3.9By similarity)
Gene namesi
Name:Clybl
Synonyms:Clb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1916884. Clybl.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020MitochondrionSequence analysisAdd
BLAST
Chaini21 – 338318Citrate lyase subunit beta-like protein, mitochondrialPRO_0000286390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysineCombined sources
Modified residuei59 – 591N6-acetyllysineCombined sources
Modified residuei64 – 641N6-acetyllysineCombined sources
Modified residuei80 – 801N6-acetyllysine; alternateCombined sources
Modified residuei80 – 801N6-succinyllysine; alternateCombined sources
Modified residuei90 – 901N6-acetyllysine; alternateCombined sources
Modified residuei90 – 901N6-succinyllysine; alternateCombined sources
Modified residuei307 – 3071N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8R4N0.
MaxQBiQ8R4N0.
PaxDbiQ8R4N0.
PRIDEiQ8R4N0.

2D gel databases

REPRODUCTION-2DPAGEQ8R4N0.

PTM databases

iPTMnetiQ8R4N0.

Expressioni

Tissue specificityi

Detected in brown fat, brain, liver, kidney, heart, skeletal muscle and ovary (at protein level).2 Publications

Gene expression databases

BgeeiQ8R4N0.
CleanExiMM_CLYBL.
GenevisibleiQ8R4N0. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8R4N0. 1 interaction.
MINTiMINT-4119178.
STRINGi10090.ENSMUSP00000026625.

Structurei

3D structure databases

ProteinModelPortaliQ8R4N0.
SMRiQ8R4N0. Positions 42-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGUQ. Eukaryota.
COG2301. LUCA.
GeneTreeiENSGT00390000017163.
HOGENOMiHOG000242281.
HOVERGENiHBG059382.
InParanoidiQ8R4N0.
KOiK11390.
OMAiEIYTPTK.
OrthoDBiEOG793B83.
PhylomeDBiQ8R4N0.
TreeFamiTF313596.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR011206. Citrate_lyase_beta/mcl1/mcl2.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFiPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8R4N0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALCVLRNTV RGAAALPRLK ASHVVSVYKP RYSSLSNHKY VPRRAVLYVP
60 70 80 90 100
GNDEKKIRKI PSLKVDCAVL DCEDGVAENK KNEARLRIAK TLEDFDLGTT
110 120 130 140 150
EKCVRINSVS SGLAEVDLET FLQARVLPSS LMLPKVEGPE EIRWFSDKFS
160 170 180 190 200
LHLKGRKLEQ PMNLIPFVET AMGLLNFKAV CEETLKTGPQ VGLCLDAVVF
210 220 230 240 250
GGEDFRASIG ATSNKDTQDI LYARQKVVVT AKAFGLQAID LVYIDFRDED
260 270 280 290 300
GLLRQSREAA AMGFTGKQVI HPNQIAVVQE QFTPTPEKIQ WAEELIAAFK
310 320 330
EHQQLGKGAF TFRGSMIDMP LLKQAQNIVT LATSIKEK
Length:338
Mass (Da):37,549
Last modified:May 1, 2007 - v2
Checksum:i6F8AA53D9EDC3958
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91T → A in AAL84704 (PubMed:11741334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428254 mRNA. Translation: AAL84704.1.
AK009345 mRNA. Translation: BAB26232.1.
BC023398 mRNA. Translation: AAH23398.1.
CCDSiCCDS27346.1.
RefSeqiNP_083832.2. NM_029556.3.
UniGeneiMm.34608.

Genome annotation databases

EnsembliENSMUST00000026625; ENSMUSP00000026625; ENSMUSG00000025545.
GeneIDi69634.
KEGGimmu:69634.
UCSCiuc007vax.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428254 mRNA. Translation: AAL84704.1.
AK009345 mRNA. Translation: BAB26232.1.
BC023398 mRNA. Translation: AAH23398.1.
CCDSiCCDS27346.1.
RefSeqiNP_083832.2. NM_029556.3.
UniGeneiMm.34608.

3D structure databases

ProteinModelPortaliQ8R4N0.
SMRiQ8R4N0. Positions 42-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R4N0. 1 interaction.
MINTiMINT-4119178.
STRINGi10090.ENSMUSP00000026625.

PTM databases

iPTMnetiQ8R4N0.

2D gel databases

REPRODUCTION-2DPAGEQ8R4N0.

Proteomic databases

EPDiQ8R4N0.
MaxQBiQ8R4N0.
PaxDbiQ8R4N0.
PRIDEiQ8R4N0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026625; ENSMUSP00000026625; ENSMUSG00000025545.
GeneIDi69634.
KEGGimmu:69634.
UCSCiuc007vax.2. mouse.

Organism-specific databases

CTDi171425.
MGIiMGI:1916884. Clybl.

Phylogenomic databases

eggNOGiENOG410IGUQ. Eukaryota.
COG2301. LUCA.
GeneTreeiENSGT00390000017163.
HOGENOMiHOG000242281.
HOVERGENiHBG059382.
InParanoidiQ8R4N0.
KOiK11390.
OMAiEIYTPTK.
OrthoDBiEOG793B83.
PhylomeDBiQ8R4N0.
TreeFamiTF313596.

Enzyme and pathway databases

BRENDAi4.1.3.6. 3474.

Miscellaneous databases

ChiTaRSiClybl. mouse.
NextBioi329946.
PROiQ8R4N0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R4N0.
CleanExiMM_CLYBL.
GenevisibleiQ8R4N0. MM.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR011206. Citrate_lyase_beta/mcl1/mcl2.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFiPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of novel mouse and human putative citrate lyase beta-subunit."
    Morikawa J., Nishimura Y., Uchida A., Tanaka T.
    Biochem. Biophys. Res. Commun. 289:1282-1286(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-90 AND LYS-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-59; LYS-64; LYS-80 AND LYS-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "CLYBL is a polymorphic human enzyme with malate synthase and beta-methylmalate synthase activity."
    Strittmatter L., Li Y., Nakatsuka N.J., Calvo S.E., Grabarek Z., Mootha V.K.
    Hum. Mol. Genet. 23:2313-2323(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCLYBL_MOUSE
AccessioniPrimary (citable) accession number: Q8R4N0
Secondary accession number(s): Q9D7D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: March 16, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

This organism lacks the other subunits that are necessary for ATP-independent citrate lyase activity. Even though this protein has clear similarity to citrate lyase beta subunit, it is expected to have a somewhat different enzyme activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.